Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis

Aneesh Goyal, Malikmohamed Yousuf, Eerappa Rajakumara, Pooja Arora, Rajesh S. Gokhale, Rajan Sankaranarayanan

Research output: Contribution to journalArticle

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Abstract

FadD28 from Mycobacterium tuberculosis belongs to the fatty-acyl AMP ligase (FAAL) family of proteins. It is essential for the biosynthesis of a virulent phthiocerol dimycocerosate (PDIM) lipid that is only found in the cell wall of pathogenic mycobacteria. The N-terminal domain, comprising of the first 460 residues, was crystallized by the hanging-drop vapour-diffusion method at 295 K. The crystals belong to space group P212121, with unit-cell parameters a = 50.97, b = 60.74, c = 136.54 Å. The crystal structure of the N-terminal domain of FadD28 at 2.35 Å resolution has been solved using the MAD method.

Original languageEnglish (US)
Pages (from-to)350-352
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue number4
DOIs
Publication statusPublished - Apr 1 2006

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ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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